TPS5A_MAIZE
ID TPS5A_MAIZE Reviewed; 554 AA.
AC Q6JD70;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Sesquithujene synthase A {ECO:0000303|PubMed:15075399};
DE EC=4.2.3.102 {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:21607717, ECO:0000269|PubMed:25940560};
DE AltName: Full=(S)-beta-bisabolene synthase {ECO:0000303|PubMed:15075399};
DE EC=4.2.3.55 {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:21607717, ECO:0000269|PubMed:25940560};
DE AltName: Full=(Z)-alpha-bergamotene synthase {ECO:0000303|PubMed:15075399};
DE EC=4.2.3.54 {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
DE AltName: Full=Beta-curcumene synthase {ECO:0000303|PubMed:15075399};
DE EC=4.2.3.- {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
DE AltName: Full=Beta-farnesene synthase {ECO:0000303|PubMed:15075399};
DE EC=4.2.3.47 {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
DE AltName: Full=Gamma-curcumene synthase {ECO:0000303|PubMed:15075399};
DE EC=4.2.3.94 {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
DE AltName: Full=Sesquisabinene B synthase {ECO:0000303|PubMed:15075399};
DE EC=4.2.3.- {ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
DE AltName: Full=Terpene synthase 5 {ECO:0000303|PubMed:15075399};
DE Short=tps5-Del1 {ECO:0000303|PubMed:15075399};
GN Name=TPS5A {ECO:0000303|PubMed:15075399};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP 3D-STRUCTURE MODELING, MUTAGENESIS OF SER-407; GLY-409; ALA-410; ASN-411
RP AND VAL-455, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Delprim;
RX PubMed=15075399; DOI=10.1105/tpc.019877;
RA Koellner T.G., Schnee C., Gershenzon J., Degenhardt J.;
RT "The variability of sesquiterpenes emitted from two Zea mays cultivars is
RT controlled by allelic variation of two terpene synthase genes encoding
RT stereoselective multiple product enzymes.";
RL Plant Cell 16:1115-1131(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21607717; DOI=10.1007/s10886-011-9967-7;
RA Fontana A., Held M., Fantaye C.A., Turlings T.C., Degenhardt J.,
RA Gershenzon J.;
RT "Attractiveness of constitutive and herbivore-induced sesquiterpene blends
RT of maize to the parasitic wasp Cotesia marginiventris (Cresson).";
RL J. Chem. Ecol. 37:582-591(2011).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25940560; DOI=10.1039/c5ob00711a;
RA Vattekkatte A., Gatto N., Koellner T.G., Degenhardt J., Gershenzon J.,
RA Boland W.;
RT "Substrate geometry controls the cyclization cascade in multiproduct
RT terpene synthases from Zea mays.";
RL Org. Biomol. Chem. 13:6021-6030(2015).
RN [4]
RP REVIEW.
RX PubMed=30187155; DOI=10.1007/s00425-018-2999-2;
RA Block A.K., Vaughan M.M., Schmelz E.A., Christensen S.A.;
RT "Biosynthesis and function of terpenoid defense compounds in maize (Zea
RT mays).";
RL Planta 249:21-30(2019).
CC -!- FUNCTION: Sesquiterpene synthase involved in the production after
CC herbivore attack of a blend of volatiles that attracts natural enemies
CC of herbivores (PubMed:15075399, PubMed:21607717). Converts farnesyl
CC diphosphate to sesquithujene, (S)-beta-bisabolene, (Z)-alpha-
CC bergamotene, sesquisabinene B and several minor products
CC (PubMed:25940560, PubMed:15075399, PubMed:21607717). Can also act in
CC vitro as a monoterpene synthase, converting geranyl diphosphate to (S)-
CC (-)-limonene, beta-myrcene and 11 other monoterpenes (PubMed:25940560,
CC PubMed:15075399). {ECO:0000269|PubMed:15075399,
CC ECO:0000269|PubMed:21607717, ECO:0000269|PubMed:25940560}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + sesquithujene;
CC Xref=Rhea:RHEA:31991, ChEBI:CHEBI:33019, ChEBI:CHEBI:63711,
CC ChEBI:CHEBI:175763; EC=4.2.3.102;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:21607717,
CC ECO:0000269|PubMed:25940560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31992;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:21607717,
CC ECO:0000269|PubMed:25940560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = (1S,5S,6S)-alpha-bergamotene +
CC diphosphate; Xref=Rhea:RHEA:30471, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:60374, ChEBI:CHEBI:61679; EC=4.2.3.54;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30472;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene +
CC diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (S)-beta-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:28266, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49263, ChEBI:CHEBI:175763; EC=4.2.3.55;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:21607717,
CC ECO:0000269|PubMed:25940560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28267;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:21607717,
CC ECO:0000269|PubMed:25940560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6E)-farnesyl diphosphate = (-)-beta-curcumene +
CC diphosphate; Xref=Rhea:RHEA:31419, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:62760, ChEBI:CHEBI:162247;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31420;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + gamma-curcumene;
CC Xref=Rhea:RHEA:32031, ChEBI:CHEBI:33019, ChEBI:CHEBI:63696,
CC ChEBI:CHEBI:175763; EC=4.2.3.94;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32032;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + sesquisabinene B;
CC Xref=Rhea:RHEA:60016, ChEBI:CHEBI:33019, ChEBI:CHEBI:143550,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:15075399,
CC ECO:0000269|PubMed:25940560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60017;
CC Evidence={ECO:0000269|PubMed:15075399, ECO:0000269|PubMed:25940560};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15075399};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15075399};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:Q5GJ60};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:30187155}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the husk. Detected in leaves.
CC {ECO:0000269|PubMed:15075399}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000250|UniProtKB:A0A1C9J6A7}.
CC -!- MISCELLANEOUS: The allele found in cv. B73 encodes an inactive enzyme
CC while the two alleles found in cv. Delprim encode an active (TPS5A) and
CC an inactive (TPS5B) enzyme (PubMed:15075399).
CC {ECO:0000305|PubMed:15075399}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AY518313; AAS88574.1; -; mRNA.
DR AlphaFoldDB; Q6JD70; -.
DR SMR; Q6JD70; -.
DR PRIDE; Q6JD70; -.
DR MaizeGDB; 1219892; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q6JD70; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0102060; F:endo-alpha-bergamotene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102064; F:gamma-curcumene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0102304; F:sesquithujene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Plant defense;
KW Reference proteome.
FT CHAIN 1..554
FT /note="Sesquithujene synthase A"
FT /id="PRO_0000418851"
FT REGION 407..411
FT /note="Determine the stereoselectivity of the enzyme"
FT MOTIF 308..312
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 452
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT MUTAGEN 407
FT /note="S->T: No effect on the product profile. Production
FT of (S)-beta-bisabolene and 7-epi-sesquithujene; when
FT associated with A-409, T-410 and I-411."
FT /evidence="ECO:0000269|PubMed:15075399"
FT MUTAGEN 409
FT /note="G->A: Altered product specificity and production of
FT mostly (S)-beta-bisabolene. Formation of 7-epi-
FT sesquithujene and sesquisabinene A; when associated with T-
FT 410. Production of (S)-beta-bisabolene and 7-epi-
FT sesquithujene; when associated with T-407, T-410 and I-
FT 411."
FT /evidence="ECO:0000269|PubMed:15075399"
FT MUTAGEN 410
FT /note="A->T: No effect on the product profile. Formation of
FT (S)-beta-bisabolene, 7-epi-sesquithujene and sesquisabinene
FT A; when associated with A-409. Production of (S)-beta-
FT bisabolene and 7-epi-sesquithujene; when associated with T-
FT 407, A-409 and I-411."
FT /evidence="ECO:0000269|PubMed:15075399"
FT MUTAGEN 411
FT /note="N->I: No effect on the product profile. Production
FT of (S)-beta-bisabolene and 7-epi-sesquithujene; when
FT associated with T-407, A-409 and T-410."
FT /evidence="ECO:0000269|PubMed:15075399"
FT MUTAGEN 455
FT /note="V->E: 60% activity and increased proportion of (E)-
FT beta-farnesene."
FT /evidence="ECO:0000269|PubMed:15075399"
SQ SEQUENCE 554 AA; 63778 MW; 4CAD6C7D746AE023 CRC64;
MASPPAHRSS KAADEELPKA SSTFHPSLWG SFFLTYQPPT APQRANMKER AEVLRERVRK
VLKGSTTDQL PETVNLILTL QRLGLGYYYE NEIDKLLHQI YSNSDYNEKD LNLVSQRFYL
LRKNGYDVPS DVFLNFKTEE GGFACAAADT RSLLSLYNAA YLRKHGEEVL DEAISSTRLR
LQDLLGRLLP ESPFAKEVSS SLRTPLFRRV GILEARNYIP IYEKEATRNE AVLELAKLNF
NLQQLDFCEE LKHCSAWWNE MIAKSKLTFV RDRIVEEYFW MNGACCDPPY SLSRIILTKI
TGLITIIDDM FDTHGTTEDC MKFAEAFGRW DESAIHLLPE YMKDFYILML ETFQSFEDAL
GPEKSYRVLY LKQAMERLVE LYSKEIKWRD QDYVATMSEH LQVSAESIGA NALTCSAYAG
MGDMSITKET FEWALSFPQF IRTFGSFVRL SNDVVSTKRE QTKDHSPSTV HCYMKEHGTT
MDDACEKIKE LIEDSWKDML EQSLALKGLP KVVPQLVFDF SRTTDNMYRD RDALTSSEAL
KEMIQLLFVE PIPE
